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Structure paper

TitleFrsA functions as a cofactor-independent decarboxylase to control metabolic flux.
Journal, issue, pagesNat. Chem. Biol., Vol. 7, Page 434-436, Year 2011
Publish dateMay 4, 2010 (structure data deposition date)
AuthorsLee, K.J. / Jeong, C.S. / An, Y.J. / Lee, H.J. / Park, S.J. / Seok, Y.J. / Kim, P. / Lee, J.H. / Lee, K.H. / Cha, S.S.
External linksNat. Chem. Biol. / PubMed:21623357
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-3mve:
Crystal structure of a novel pyruvate decarboxylase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3our:
Crystal structure of complex between EIIA and a novel pyruvate decarboxylase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • vibrio vulnificus (bacteria)
KeywordsLYASE / FrsA / fermentation/respiration switch protein / hydrolase activator / LYASE/TRANSFERASE / exhibit no hydrolase activity1 / LYASE-TRANSFERASE complex

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